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. 2001 Feb;3(2):193-7.
doi: 10.1038/35055104.

Protein S-nitrosylation: a physiological signal for neuronal nitric oxide

S R Jaffrey  1 , H Erdjument-Bromage, C D Ferris, P Tempst, S H Snyder
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Protein S-nitrosylation: a physiological signal for neuronal nitric oxide

S R Jaffrey et al. Nat Cell Biol. 2001 Feb.

Abstract

Nitric oxide (NO) has been linked to numerous physiological and pathophysiological events that are not readily explained by the well established effects of NO on soluble guanylyl cyclase. Exogenous NO S-nitrosylates cysteine residues in proteins, but whether this is an important function of endogenous NO is unclear. Here, using a new proteomic approach, we identify a population of proteins that are endogenously S-nitrosylated, and demonstrate the loss of this modification in mice harbouring a genomic deletion of neuronal NO synthase (nNOS). Targets of NO include metabolic, structural and signalling proteins that may be effectors for neuronally generated NO. These findings establish protein S-nitrosylation as a physiological signalling mechanism for nNOS.

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Comment in

  • S-nitrosylation: spectrum and specificity.
    Hess DT, Matsumoto A, Nudelman R, Stamler JS. Hess DT, et al. Nat Cell Biol. 2001 Feb;3(2):E46-9. doi: 10.1038/35055152. Nat Cell Biol. 2001. PMID: 11175760 No abstract available.

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